| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase FAP |
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| Ligand | BDBM50399730 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_876940 (CHEMBL2185388) |
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| IC50 | >100000±n/a nM |
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| Citation |  Van der Veken, P; Fülöp, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K P2-substituted N-acylprolylpyrrolidine inhibitors of prolyl oligopeptidase: biochemical evaluation, binding mode determination, and assessment in a cellular model of synucleinopathy. J Med Chem55:9856-67 (2012) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Prolyl endopeptidase FAP |
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| Name: | Prolyl endopeptidase FAP |
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| Synonyms: | Fap | Fibroblast activation protein (FAP) | SEPR_MOUSE | Seprase |
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| Type: | Enzyme |
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| Mol. Mass.: | 87949.14 |
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| Organism: | Mus musculus (Mouse) |
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| Description: | P97321 |
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| Residue: | 761 |
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| Sequence: | MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPN
WISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSK
LWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPP
FQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYG
DGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVS
SERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQD
ATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPG
RRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGR
TDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQV
YGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQ
LTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIY
SERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNA
QVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD
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| BDBM50399730 |
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| n/a |
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| Name | BDBM50399730 |
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| Synonyms: | CHEMBL2178967 |
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| Type | Small organic molecule |
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| Emp. Form. | C27H30BrN5O2 |
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| Mol. Mass. | 536.463 |
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| SMILES | Brc1ccc(cc1)-c1cn(nn1)[C@H]1C[C@H](N(C1)C(=O)CCCc1ccccc1)C(=O)N1CCCC1 |r| |
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| Structure | 
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